Crystal structure of Plasmodium berghei actin I with D-loop from muscle actin. Determined by X-ray diffraction at 2.5 Å resolution. Released 30 Apr 2014.
Explore 4CBW in 3D Show helices and sheets RCSB PDB PDBe
4CBW contains 33 α-helices and 28 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-8 | 2 | |
| β-strand | 9-12 | 4 | 1 |
| β-strand | 17-22 | 6 | 1 |
| β-strand | 30-33 | 4 | 1 |
| β-strand | 36-39 | 4 | 2 |
| β-strand | 54-55 | 2 | 2 |
| α-helix | 57-60 | 4 | |
| α-helix | 63-65 | 3 | |
| β-strand | 66-69 | 4 | 2 |
| β-strand | 72-73 | 2 | 3 |
| β-strand | 76-77 | 2 | 3 |
| α-helix | 80-88 | 9 | |
| α-helix | 89-95 | 7 | |
| α-helix | 99-101 | 3 | |
| β-strand | 104-108 | 5 | 1 |
| α-helix | 114-126 | 13 | |
| β-strand | 132-137 | 6 | 1 |
| α-helix | 138-145 | 8 | |
| β-strand | 151-156 | 6 | 4 |
| β-strand | 161-167 | 7 | 4 |
| β-strand | 170-171 | 2 | 4 |
| α-helix | 173-175 | 3 | |
| β-strand | 177-179 | 3 | 4 |
| α-helix | 183-193 | 11 | |
| α-helix | 194-197 | 4 | |
| α-helix | 206-217 | 12 | |
| β-strand | 219 | 1 | 5 |
| α-helix | 224-233 | 10 | |
| β-strand | 239-242 | 4 | 6 |
| β-strand | 248-251 | 4 | 6 |
| α-helix | 254-257 | 4 | |
| α-helix | 259-262 | 4 | |
| α-helix | 265-268 | 4 | |
| α-helix | 272-274 | 3 | |
| α-helix | 275-284 | 10 | |
| α-helix | 288-290 | 3 | |
| α-helix | 291-295 | 5 | |
| β-strand | 298-301 | 4 | 4 |
| α-helix | 303-306 | 4 | |
| β-strand | 308 | 1 | 5 |
| α-helix | 310-321 | 12 | |
| β-strand | 330-331 | 2 | 4 |
| α-helix | 339-347 | 9 | |
| α-helix | 353-355 | 3 | |
| β-strand | 358-359 | 2 | 1 |
| α-helix | 360-366 | 7 | |
| α-helix | 368-370 | 3 | |
| α-helix | 371-374 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 30-34 | 5 | |
| β-strand | 40-46 | 7 | 7 |
| β-strand | 51-53 | 3 | 7 |
| α-helix | 54-55 | 2 | |
| α-helix | 56-58 | 3 | |
| β-strand | 61-63 | 3 | 8 |
| β-strand | 67-75 | 9 | 7 |
| β-strand | 81-89 | 9 | 7 |
| α-helix | 95-111 | 17 | |
| β-strand | 116-122 | 7 | 7 |
| α-helix | 128-131 | 4 | |
| β-strand | 139-141 | 3 | 8 |
| α-helix | 145-147 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin, alpha skeletal muscle, actin | A | protein | 377 | PLASMODIUM BERGHEI, SYNTHETIC CONSTRUCT | P68137 (AlphaFold model), Q4Z1L3 (AlphaFold model) |
| Gelsolin | G | protein | 127 | MUS MUSCULUS | P13020 (AlphaFold model) |
>4CBW_1 ACTIN, ALPHA SKELETAL MUSCLE, ACTIN (chains A) GAGDEEVQALVIDNGSGNVKAGVAGDDAPRSVFPSIVGRPRHQGVMVGMGQKDSYVGDEA QSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRAAPEEHPVLLTEAPLNPKGNRER MTQIMFESFNVPAMYVAIQAVLSLYSSGRTTGIVLDSGDGVSHTVPIYEGYALPHAIMRL DLAGRDLTEYLMKILHERGYGFSTSAEKEIVRDIKEKLCYIALNFDEEMKTSEQSSDIEK SYELPDGNIITVGNERFRCPEALFQPSFLGKEAAGIHTTTFNSIKKCDVDIRKDLYGNIV LSGGTTMYEGIGERLTRDITTLAPSTMKIKVVAPPERKYSVWIGGSILSSLSTFQQMWIT KEEYDESGPSIVHRKCF
>4CBW_2 GELSOLIN (chains G) GPMVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPPNLYGDFFTGDAYVILKTVQLRNGNLQ YDLHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESSTFSGYFKSGLKYKK GGVASGF
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 3 |
| DIO | 1,4-diethylene dioxide | C4 H8 O2 | 1 |
| ATP | Adenosine-5'-triphosphate | C10 H16 N5 O13 P3 | 1 |
Structural Differences Explain Diverse Functions of Plasmodium Actins. Vahokoski, J., Bhargav, S.P., Desfosses, A. et al. PLoS Pathog (2014) 10:4091. DOI 10.1371/JOURNAL.PPAT.1004091 · PubMed
Other PDB entries of the same protein (UniProt P68137 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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